ArticleJournal of virology2013
Identification of a region in the stalk domain of the nipah virus receptor binding protein that is critical for fusion activation.
Article in Journal of virology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 22 citations in OpenAlex.
- Structure-guided mutagenesis of Henipavirus receptor-binding proteins reveals molecular determinants of receptor usage and antibody-binding epitopes.Journal of virology · 2024Article
- Subnanometer structure of an enveloped virus fusion complex on viral surface reveals new entry mechanisms.Science advances · 2023Article
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- Transmembrane Domains of Highly Pathogenic Viral Fusion Proteins Exhibit Trimeric AssociationmSphere · 2018Article
- Monomeric ephrinB2 binding induces allosteric changes in Nipah virus G that precede its full activation.Nature communications · 2017Article
- TMPRSS12 Is an Activating Protease for Subtype B Avian Metapneumovirus.Journal of virology · 2016Article
- Stimulation of Nipah Fusion: Small Intradomain Changes Trigger Extensive Interdomain Rearrangements.Biophysical journal · 2016Article
- Integrin αvβ1 Modulation Affects Subtype B Avian Metapneumovirus Fusion Protein-mediated Cell-Cell Fusion and Virus Infection.The Journal of biological chemistry · 2016Article
- Trypsin- and low pH-mediated fusogenicity of avian metapneumovirus fusion proteins is determined by residues at positions 100, 101 and 294.Scientific reports · 2015Article
- Sequential conformational changes in the morbillivirus attachment protein initiate the membrane fusion process.PLoS pathogens · 2015Article
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- Unity in diversity: shared mechanism of entry among paramyxoviruses.Progress in molecular biology and translational science · 2015Review
- The measles virus hemagglutinin stalk: structures and functions of the central fusion activation and membrane-proximal segments.Journal of virology · 2014Article
- Structural basis of efficient contagion: measles variations on a theme by parainfluenza viruses.Current opinion in virology · 2014Review
- Measles virus fusion machinery activated by sialic acid binding globular domain.Journal of virology · 2013Article
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
Paramyxoviruses, including the emerging lethal human Nipah virus (NiV) and the avian Newcastle disease virus (NDV), enter host cells through fusion of the viral and target cell membranes. For paramyxoviruses, membrane fusion is the result of the concerted action of two viral envelope glycoproteins: a receptor binding protein and a fusion protein (F). The NiV receptor binding protein (G) attaches to ephrin B2 or B3 on host cells, whereas the corresponding hemagglutinin-neuraminidase (HN) attachment protein of NDV interacts with sialic acid moieties on target cells through two regions of its globular domain. Receptor-bound G or HN via its stalk domain triggers F to undergo the conformational changes that render it competent to mediate fusion of the viral and cellular membranes. We show that chimeric proteins containing the NDV HN receptor binding regions and the NiV G stalk domain require a specific sequence at the connection between the head and the stalk to activate NiV F for fusion. Our findings are consistent with a general mechanism of paramyxovirus fusion activation in which the stalk domain of the receptor binding protein is responsible for F activation and a specific connecting region between the receptor binding globular head and the fusion-activating stalk domain is required for transmitting the fusion signal.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.